. In the experiments of Barrick, et al. ( observed that replacement of histidine by a noncovalently bonded imidazole not only reduced cooperativity but also increased the oxy- gen affinity of the hemoglobin. Suggest an explanation. it was
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- The anticlotting property of heparin is partly the result of the negative charges it carries. ( Q.) Which type of heparin is a better anticoagulant, one with a high or a low degree of polymerization?2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?2. (a) The binding site of 2,3-bisphosphoglycerate (BPG) (red stick figure) in the deoxyhemo- globin molecule is illustrated below. Note that the two phosphate groups and the carboxylate group of the BPG molecule confer strong, negative electrostatic character to the molecule. B₁-subunit 1. 2. 3. 5. 6. B₁ (b) Mutant Hemoglobin Hb Raleigh Hb Helsinki The mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or in the vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for binding BPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for Hb Raleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substituted by Ala. Hb Rahere Hb Rancho Mirage Hb Little Rock B₂ Hb Ohio Mutation Val (31)Ala Lys(382) Met Lys(382)) Thr His(143)Asp His(3143)Gln a-NHẠ Ala(142)Asp His 2 His 143 BPG His 143 Lys 82 His 2 Rank the affinity of the mutant hemoglobins for…
- . What physiological effect would you predict from a mutation that replaced with serine the cysteine in the constant part of the immunoglobulin light chain that is involved in disulfide-bond for- mation with the heavy chain? ,List 4 different actiated carrier molecules, for each one, list both the oxided and reduced formsPlease fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to the
- Certain antibodies have been shown to bind only to the folded structure oftheir target protein ligand; yet others will bind to both the folded and denatured states of the same protein ligand. Explain this observation.. What would you predict to be the relative rate of synonymous and nonsynonymous substitutions in a globinpseudogene?The steps involved in the T→ R transition in when oxygen binds to hemoglobin are outlined below. Place them in the correct order (1 = first thing to happen), assuming that it is the oxygen-binding that initiates the transition and that the process occurs in discrete steps. The proximal histidine is pulled by the heme iron. The F helix is pulled out of place, breaking a network of salt bridges. The iron is pulled into the plane of the protoporphyrin IX ring. Oxygen binds to the heme. < <
- In a molecular disease of hemoglobin, Hemoglobin Rainier, Tyr 145β is replaced by Cys, which forms a disulfide bond with another Cysresidue in the same subunit. This prevents the formation of ion pairs that normally stabilize the T state. How does hemoglobin Rainier differ from normal hemoglobin with respect to (A)oxygen affinity, (B)the Bohr effect, and (C)the Hillcoefficient? Explain your answers.There are almost 500 naturally occurring variants of hemoglobin. Most are the result of a single amino acid substitution in a globin polypeptide chain. Some variants produce clinical illness, though not all variants have deleterious effects. A brief sample follows. HbS (sickle-cell Hb): substitutes a Val for a Glu on the surface Hb Cowtown: eliminates an ion pair involved in T-state stabilization Hb Memphis: substitutes one uncharged polar residue for another of similar size on the surface Hb Bibba: substitutes a Pro for a Leu involved in an _ helix Hb Milwaukee: substitutes a Glu for a Val Hb Providence: substitutes an Asn for a Lys that normally projects into the central cavity of the tetramer Hb Philly: substitutes a Phe for a Tyr, disrupting hydrogen bonding at the alß1 interface Explain your choices for each of the following: (a) The Hb variant least likely to cause pathological symptoms. (b) The variant(s) most likely to show pI values different from that of HbA. (c) The…Suggest probable consequences of the following real or possible hemoglobinmutations. [Note: as shown](a) At β146 (HC3) His → Asp(b) At β92 (F8) His → LeuIn each case, indicate whether a single-nucleotide change is sufficient forthe mutation.